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  • Title: Characterization of purified c-type heme-containing peptides and identification of c-type heme-attachment sites in Shewanella oneidenis cytochromes using mass spectrometry.
    Author: Yang F, Bogdanov B, Strittmatter EF, Vilkov AN, Gritsenko M, Shi L, Elias DA, Ni S, Romine M, Pasa-Tolić L, Lipton MS, Smith RD.
    Journal: J Proteome Res; 2005; 4(3):846-54. PubMed ID: 15952731.
    Abstract:
    We describe methods for mass spectrometric identification of heme-containing peptides from c-type cytochromes that contain the CXXCH (X=any amino acid) sequence motif. The heme fragment ion yielded the most abundant MS/MS peak for standard heme-containing peptides with one amino acid difference for both 2+ and 3+ peptide charge states; both sequence and charge affect the extent of heme loss. Application to Shewanella oneidenis demonstrated the utility of this approach for identifying c-type heme-containing peptides from complex proteome samples.
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